A novel silk-based segmented block copolymer containing GlyAlaGlyAla ?-sheets templated by phenoxathiin

Rathore, Osman; Winningham, Michael J.; Sogah, Dotsevi Y.

doi:10.1002/(sici)1099-0518(20000115)38:2<352::aid-pola10>3.0.co;2-p

Cited by 37 publications

(56 citation statements)

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“…[3][4][5] A further interesting example in this context is the work by Sogah et al, who have investigated segmented multiblock copolymers composed of silk-based R-amino acid sequences and PEG, which were prepared via polycondensation. [6][7][8] In addition to dilute solution properties, a further question, especially taking into account the amorphous or semicrystalline nature of most synthetic polymers, is whether the selfassembly properties of the peptide sequences are also retained in the solid state/melt upon conjugation to a synthetic macromolecule. If this is the case, then attachment of welldefined peptide sequences to synthetic macromolecules may be a versatile strategy to generate novel polymeric materials with unprecedented nanoscale order.…”

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confidence: 99%

“…In the WAXS pattern, two strong characteristic peaks of PEG crystallized in a monoclinic unit cell can be recognized at low temperature. 15 These peaks are listed in Table 1 as d 6 , which was indexed as the 120 reflection, and d 8 , which was indexed as an overlap of 112, 032, 1 h32, and 2 h12 reflections. The peak labeled d 5 corresponds to the 020 reflection observed in the orthorhombic unit cell containing antiparallel -sheets in poly(L-alanylglycine).…”

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Nanoscale Structure of Poly(Ethylene Glycol) Hybrid Block Copolymers containing Amphiphilic β-Strand Peptide Sequences

et al. 2003

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This paper discusses the solid state and melt nanoscale structure of a series of novel poly(ethylene glycol) (PEG) hybrid di- and triblock copolymers, which contain amphiphilic beta-strand peptide sequences. The block copolymers have been prepared via solid-phase synthesis, affording perfectly monodisperse peptide segments with a precisely defined alpha-amino acid sequence. Attenuated total reflection Fourier transform infrared spectroscopy and X-ray scattering experiments indicate that the self-assembly properties of the peptide sequences are retained upon conjugation to PEG and mediate the formation of an ordered superstructure consisting of alternating PEG layers and peptide domains with an highly organized antiparallel beta-sheet structure. The results suggest that combination of biological structural motifs with synthetic polymers may be a versatile strategy for the development of novel self-assembled materials with complex internal structures and the potential to interface with biology.

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Nanoscale Structure of Poly(Ethylene Glycol) Hybrid Block Copolymers containing Amphiphilic β-Strand Peptide Sequences

et al. 2003

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“…In another approach, Sogah et al prepared segmented block copolymers containing PEG segments and the Gly‐Ala‐Gly‐Ala peptide sequence derived from B. mori silk, templated by phenoxathiin (Figure 3). 32–34 The peptide segment retained its β ‐sheet structure, and transmission electron microscopy (TEM) experiments showed that it was dispersed in a continuous polyether phase. Thus, selectively exchanging or modifying certain segments of naturally occurring biopolymers with a judiciously selected synthetic polymer while, at the same time, retaining other segments known to be critical for the essential properties of the native biopolymer, can result in a peptide/protein‐polymer conjugate with similar (or better) properties and function.…”

Section: Controlling Nanoscale Structure Formationmentioning

confidence: 99%

“… Natural silk mimics: a) multiblock copolymer consisting of PEG as the soft linker and natural β ‐sheet sequences ([Ala] 4‐8 ); b) segmented block copolymer consisting of soft EG segments and Gly‐Ala‐Gly‐Ala β ‐sheets, templated by phenoxathiin. (Adapted from ref 33…”

Section: Controlling Nanoscale Structure Formationmentioning

confidence: 99%

Peptide/Protein Hybrid Materials: Enhanced Control of Structure and Improved Performance through Conjugation of Biological and Synthetic Polymers

Vandermeulen¹,

Klok²

2004

Macromolecular Bioscience

244

239

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The conjugation of peptides/proteins and synthetic polymers is a useful strategy to overcome some of the limitations related to the use of the individual components. This review will highlight two aspects: enhanced structural control at the nanometer level and improved performance, in particular with respect to biomedical applications. In the former case, peptide sequences are mainly used to mediate self-assembly of synthetic polymers. In the latter case, conjugation of an appropriate synthetic polymer to a pharmaceutically active peptide/protein can, for example, prevent premature enzymatic degradation and enhance blood circulation times, which is therapeutically advantageous.

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“…Only few examples have been reported in which small peptidic elements have been used in the preparation of "hybrid" multiblock copolymers. An interesting example in which the peptide segment was used to contribute to the mechanical properties of the final material is the work of Sogah et al [26][27][28]. They prepared Bombyx mori silk worm silk and Nephila clavipes spider dragline silk mimetic block copolymers.…”

Section: Solution Phase Synthesis Of Peptide-containing Block Copolymersmentioning

confidence: 99%

Peptide-Containing Block Copolymers: Synthesis and Potential Applications of Bio-Mimetic Materials

Smeenk

Löwik²,

Hest

2005

COC

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The progress in both peptide and polymer chemistry has led to the preparation of "hybrids" to yield compounds with properties not achievable with the separate components. In this review we aim at describing the current synthetic methodologies for the preparation of peptide containing block copolymers, either being completely peptidic or as hybrids with synthetic polymer blocks. The different techniques to prepare these polymers are ordered by level of control over peptide sequence and hence their molecular structure. First, recent developments in NCA polymerization will be discussed, which enable the construction of well-defined high molecular weight peptide based block copolymers, albeit with no absolute control over amino acid composition. Solution phase peptide synthesis allows the preparation of small peptide sequences, which can be incorporated into the side chain or the main chain of hybrid polymer architectures. Application of solid phase peptide synthesis and the newly developed peptide ligation methods has resulted in an extension of the length of the peptide fragments that can be conveniently incorporated into hybrid polymer structures. Finally absolute control over amino acid sequence, combined with the ability to create high molecular weight species is accomplished with the application of protein engineering to the field of polymer science. INTRODUCTIONThe development of synthetic approaches for the preparation of well-defined polypeptide-based materials has attracted increasing attention in the polymer chemistry field. The presence of many levels of supramolecular organization present in proteinaceous materials in nature shows that only a limited number of monomer building blocks is sufficient for the construction of complex structures, with a wide range of properties. The chemical information present in the amino acid side chains does not only result in the folding of the peptide main-chain into a specific secondary structure, but is also responsible for tertiary folding as a consequence of the delicate interplay of a variety of non-covalent interactions, like hydrophobic, hydrogen-bonding and ionic interactions. Despite the large variety of monomers that can be polymerized chemically and the increasing level of control over polymer size distribution using controlled polymerization techniques [1], a fundamental limitation of synthetic polymerization methods, when compared to ribosomal protein production, is the lack of absolute control over monomer sequence.In many cases, only small peptide sequences are already sufficient to introduce specific functionality such as folding, recognition, biodegradability and mechanical properties into molecular structures. This realization has led to an increased use of polypeptide preparation methods of organic synthetic and biosynthetic origin in polymer science. Especially, the combination of amino acid sequences and synthetic (meaning non-peptidic) polymers has drawn much attention. The synthetic polymer part can either act simply as a carrier

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A novel silk-based segmented block copolymer containing GlyAlaGlyAla ?-sheets templated by phenoxathiin

Cited by 37 publications

References 38 publications

Nanoscale Structure of Poly(Ethylene Glycol) Hybrid Block Copolymers containing Amphiphilic β-Strand Peptide Sequences

Nanoscale Structure of Poly(Ethylene Glycol) Hybrid Block Copolymers containing Amphiphilic β-Strand Peptide Sequences

Peptide/Protein Hybrid Materials: Enhanced Control of Structure and Improved Performance through Conjugation of Biological and Synthetic Polymers

Peptide-Containing Block Copolymers: Synthesis and Potential Applications of Bio-Mimetic Materials

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